The conformational signature of β-arrestin2 predicts its trafficking and signalling functions

Mi-Hye Lee, Kathryn M. Appleton, Erik G. Strungs, Joshua Y. Kwon, Thomas A. Morinelli, Yuri K. Peterson, Stephane A. Laporte and Louis M. Luttrell ()
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Mi-Hye Lee: Medical University of South Carolina
Kathryn M. Appleton: Medical University of South Carolina
Erik G. Strungs: Medical University of South Carolina
Joshua Y. Kwon: Medical University of South Carolina
Thomas A. Morinelli: Medical University of South Carolina
Yuri K. Peterson: College of Pharmacy, Medical University of South Carolina
Stephane A. Laporte: McGill University Health Center Research Institute, McGill University
Louis M. Luttrell: Medical University of South Carolina

Nature, 2016, vol. 531, issue 7596, 665-668

Abstract: A series of intramolecular fluorescent FlAsH BRET reporters is used to monitor conformational changes in β-arrestin2 following activation of seven G-protein-coupled receptors (GPCRs), showing that different GPCRs produce distinct β-arrestin2 conformational signatures that correlate with the stability of the receptor–arrestin complex and the role of β-arrestin2 in activating or dampening downstream signalling events, which explains how different GPCRs can use a common effector for different purposes.

Date: 2016
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DOI: 10.1038/nature17154

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